PIP27_MAIZE
ID PIP27_MAIZE Reviewed; 287 AA.
AC Q9ATM4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Aquaporin PIP2-7;
DE AltName: Full=Plasma membrane intrinsic protein 2-7;
DE AltName: Full=ZmPIP2-7;
DE AltName: Full=ZmPIP2;7;
GN Name=PIP2-7;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. B73;
RX PubMed=11244102; DOI=10.1104/pp.125.3.1206;
RA Chaumont F., Barrieu F., Wojcik E., Chrispeels M.J., Jung R.;
RT "Aquaporins constitute a large and highly divergent protein family in
RT maize.";
RL Plant Physiol. 125:1206-1215(2001).
CC -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC neutral solutes across cell membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
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DR EMBL; AF326496; AAK26763.1; -; mRNA.
DR RefSeq; NP_001105639.1; NM_001112169.1.
DR AlphaFoldDB; Q9ATM4; -.
DR SMR; Q9ATM4; -.
DR ProMEX; Q9ATM4; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9ATM4; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR45687; PTHR45687; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..287
FT /note="Aquaporin PIP2-7"
FT /id="PRO_0000286024"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..111
FT /note="NPA 1"
FT /evidence="ECO:0000250"
FT MOTIF 230..232
FT /note="NPA 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 30799 MW; 3FFB48F33954BB8C CRC64;
MAKDVEQVTE QGEYSAKDYH DPPPAPLIDP DELTKWSLYR AAIAEFIATL LFLYITVLTI
IGYKRQSDTK IPGNTECDGV GILGIAWAFG GMIFILVYCT AGISGGHINP AVTFGLFLGR
KVSLVRALLY MIAQCAGAIC GAGLAKGFQK SFYNRYGGGV NTVSDGYNKG TALGAEIIGT
FVLVYTVFSA TDPKRNARDS HVPVLAPLPI GFAVFMVHLA TIPVTGTGIN PARSFGPAVI
FNNDKAWDDQ WIYWVGPFVG AAVAAIYHQY ILRGSAIKAL GSFRSNA
